BMRB Entry 15694
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15694
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Title: Apple Domains 1 and 2 from Toxoplasma gondii microneme protein 4 PubMed: 19636884
Deposition date: 2008-03-26 Original release date: 2008-07-08
Authors: Marchant, Jan; Sawmynaden, Kovilen; Saouros, Savvas; Simpson, Peter; Matthews, Steve
Citation: Marchant, Jan; Sawmynaden, Kovilen; Saouros, Savvas; Simpson, Peter; Matthews, Stephen. "Complete resonance assignment of the first and second apple domains of MIC4 from Toxoplasma gondii, using a new NMRView-based assignment aid" Biomol. NMR Assignments 2, 119-121 (2008).
Assembly members:
MIC4_Ap12, polymer, 174 residues, 18711.6 Da.
Natural source: Common Name: Toxoplasma gondii Taxonomy ID: 5811 Superkingdom: Eukaryota Kingdom: not available Genus/species: Toxoplasma gondii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-32 Xa/LIC
Entity Sequences (FASTA):
MIC4_Ap12: SSEPAKLDLSCVHSDNKGSR
APTIGEPVPDVSLEQCAAQC
KAVDGCTHFTYNDDSKMCHV
KEGKPDLYDLTGGKTASRSC
DRSCFEQHVSYEGAPDVMTA
MVTSQSADCQAACAADPSCE
IFTYNEHDQKCTFKGRGFSA
FKERGVLGVTSGPKQFCDEG
GKLTQEEMEDQISG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 649 |
| 15N chemical shifts | 168 |
| 1H chemical shifts | 989 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | protein | 1 |
Entities:
Entity 1, protein 174 residues - 18711.6 Da.
| 1 | SER | SER | GLU | PRO | ALA | LYS | LEU | ASP | LEU | SER | ||||
| 2 | CYS | VAL | HIS | SER | ASP | ASN | LYS | GLY | SER | ARG | ||||
| 3 | ALA | PRO | THR | ILE | GLY | GLU | PRO | VAL | PRO | ASP | ||||
| 4 | VAL | SER | LEU | GLU | GLN | CYS | ALA | ALA | GLN | CYS | ||||
| 5 | LYS | ALA | VAL | ASP | GLY | CYS | THR | HIS | PHE | THR | ||||
| 6 | TYR | ASN | ASP | ASP | SER | LYS | MET | CYS | HIS | VAL | ||||
| 7 | LYS | GLU | GLY | LYS | PRO | ASP | LEU | TYR | ASP | LEU | ||||
| 8 | THR | GLY | GLY | LYS | THR | ALA | SER | ARG | SER | CYS | ||||
| 9 | ASP | ARG | SER | CYS | PHE | GLU | GLN | HIS | VAL | SER | ||||
| 10 | TYR | GLU | GLY | ALA | PRO | ASP | VAL | MET | THR | ALA | ||||
| 11 | MET | VAL | THR | SER | GLN | SER | ALA | ASP | CYS | GLN | ||||
| 12 | ALA | ALA | CYS | ALA | ALA | ASP | PRO | SER | CYS | GLU | ||||
| 13 | ILE | PHE | THR | TYR | ASN | GLU | HIS | ASP | GLN | LYS | ||||
| 14 | CYS | THR | PHE | LYS | GLY | ARG | GLY | PHE | SER | ALA | ||||
| 15 | PHE | LYS | GLU | ARG | GLY | VAL | LEU | GLY | VAL | THR | ||||
| 16 | SER | GLY | PRO | LYS | GLN | PHE | CYS | ASP | GLU | GLY | ||||
| 17 | GLY | LYS | LEU | THR | GLN | GLU | GLU | MET | GLU | ASP | ||||
| 18 | GLN | ILE | SER | GLY |
Samples:
sample_1: MIC4_Ap12, [U-100% 13C; U-100% 15N], 300 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking, structure solution
NMR spectrometers:
- Bruker DRX 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts